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首页> 外文期刊>Journal of Molecular Biology >Inositol 1,4,5-trisphosphate receptor contains multiple cavities and L-shaped ligand-binding domains.
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Inositol 1,4,5-trisphosphate receptor contains multiple cavities and L-shaped ligand-binding domains.

机译：肌醇1,4,5-三磷酸受体含有多个腔和L型配体结合结构域。

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摘要

Calcium concentrations are strictly regulated in all biological cells, and one of the key molecules responsible for this regulation is the inositol 1,4,5-trisphosphate receptor, which was known to form a homotetrameric Ca(2+) channel in the endoplasmic reticulum. The receptor is involved in neuronal transmission via Ca(2+) signaling and for many other functions that relate to morphological and physiological processes in living organisms. We analysed the three-dimensional structure of the ligand-free form of the receptor based on a single-particle technique using an originally developed electron microscope equipped with a helium-cooled specimen stage and an automatic particle picking system. We propose a model that explains the complex mechanism for the regulation of Ca(2+) release by co-agonists, Ca(2+), inositol 1,4,5-trisphosphate based on the structure of multiple internal cavities and a porous balloon-shaped cytoplasmic domain containing a prominent L-shaped density which was assigned by the X-ray structure of the inositol 1,4,5-trisphosphate binding domain.
机译：钙浓度在所有生物细胞中受到严格调节，而负责这种调节的关键分子之一是肌醇1,4,5-三磷酸受体，已知其在内质网中形成同源四聚Ca（2+）通道。该受体参与通过Ca（2+）信号传导的神经元传递和许多其他功能，这些功能与生物体的形态和生理过程有关。我们使用装备有氦冷却样品台和自动粒子采集系统的原始开发的电子显微镜，基于单粒子技术分析了无配体形式的受体的三维结构。我们提出了一个模型，该模型解释了由多个激动剂，Ca（2+），肌醇1,4,5-三磷酸酯协同激动剂调节Ca（2+）释放的复杂机制，该模型基于多个内部空腔和多孔气球的结构形的胞质结构域，具有突出的L形密度，该密度由肌醇1,4,5-三磷酸结合域的X射线结构确定。

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